Editorial: Kv7 Channels: Structure, Physiology, and Pharmacology
Thomas A. Jepps, Vincenzo Barrese, Francesco Miceli
Abstract
The Kv7 family of voltage-gated potassium (K + ) channels consists of five members (Kv7.1-7.5) encoded for by the KCNQ1-5 genes, respectively. Kv7 channels assemble as tetramers of identical or compatible subunits, with each subunit consisting of six transmembrane segments (S1-S6) and cytoplasmic N-and C-termini. The transmembrane segments between S1 and S4 form the voltage-sensing domain (VSD), where the S4 segment is crucial for channel gating as it contains positively charged arginines (Rs), each separated by non-polar residues. The S5 and S6 segments and the interconnecting loop participate to the formation of the pore domain (PD). Kv7 channels are characterized by a long intracellular C-terminus, containing domains necessary for tetramerization and involved in binding and transductional activity by critical regulators, such as phosphatidylinositol 4,5-bisphosphate (PIP2), calmodulin (CaM), syntaxin, A-kinase-anchoring proteins and proteinkinase C, and ankyrin-G (